Jijie Chai

Jijie Chai, Ph.D.  professor

B.S. Chemical Engineering, 1983-1987, Dalian Institute of Light Industry, China
M.S, Applied Chemistry, Research Institute of Petroleum Processing,
Ph.D. Medicinal Analysis, 1994-1997, Peking Union Medical College, China
2009.03-present Tsinghua University, School of Life Sceinces
2004-2009.03 National Institute of Biological Sciences, Beijing, China
1999-2004 postdoctoral fellow, Department of Molecular Biology, Princeton University, USA
1997-1999 postdoctoral fellow, Institute of Biophysics, Chinese Academy of Sciences


Research interest

The main interest of the laboratory is focused on structural and functional studies of biologically and medically important macromolecules, mainly through protein crystallography, in couple with biochemical, biological and other approaches, to gain insights into structure-function relationship of these macromolecules. Our research program embraces, but is not limited to, collaborations with the groups within National Institute of Biological Sciences, where several joint projects have been initiated. Specifically, one line of the research will be focused on the elucidation the molecular mechanisms underling transcription regulation by covalent histone modifications, especially histone methylation. Another project we are currently interested in is about pathogen-host interaction. The long-term goal of our lab is to investigate the structure-function relationship of protein involved in these two fields.

Selected publications

1.    Tang J, Han Z, Sun Y, Zhang H, Gong X, Chai J.Structural basis for recognition of an endogenous peptide by the plant receptor kinase PEPR1.Cell Res. 2015 Jan;25(1):110-20.     

2.    Song W, Han Z, Sun Y, Chai J.Crystal structure of a plant leucine rich repeat protein with two island domains.Sci China Life Sci. 2014 Jan;57(1):137-44.

3.    Li Y, Zhang L, Liu T, Chai C, Fang Q, Wu H, Agudelo Garcia PA, Han Z, Zong S, Yu Y, Zhang X, Parthun MR, Chai J, Xu RM, Yang M.Hat2p recognizes the histone H3 tail to specify the acetylation of the newly synthesized H3/H4 heterodimer by the Hat1p/Hat2p complex.Genes Dev. 2014 Jun 1;28(11):1217-27.

4.    Han Z, Sun Y, Chai J.Structural insight into the activation of plant receptor kinases.2014 Curr Opin Plant Biol. 2014 Aug;20:55-63.   

5.    Xu, C., Li, M., Wu, J., Guo, H., Li, Q., Zhang, Y., Chai, J., Li, T., and Xue, Y. (2013). Identification of a canonical SCF(SLF) complex involved in S-RNase-based self-incompatibility of Pyrus (Rosaceae). Plant Mol Biol 81, 245-257.

6.    Sun Y, Han Z, Tang J, Hu Z, Chai C, Zhou B, Chai J.Structure reveals that BAK1 as a co-receptor recognizes the BRI1-bound brassinolide.Cell Res. 2013 Nov;23(11):1326-9.

7.    Sun Y, Li L, Macho AP, Han Z, Hu Z, Zipfel C, Zhou JM, Chai J.Structural basis for flg22-induced activation of the Arabidopsis FLS2-BAK1 immune complex.Science. 2013 Nov 1;342(6158):624-8.

8.     She J, Han Z, Zhou B, Chai J.Structural basis for differential recognition of brassinolide by its receptors.Protein Cell. 2013 Jun;4(6):475-82.

9.    Hu Z, Yan C, Liu P, Huang Z, Ma R, Zhang C, Wang R, Zhang Y, Martinon F, Miao D, Deng H, Wang J, Chang J, Chai J.Crystal structure of NLRC4 reveals its autoinhibition mechanism.Science. 2013 Jul 12;341(6142):172-5.

10. Chai C, Yu Y, Zhuo W, Zhao H, Li X, Wang N, Chai J, Yang M.Structural basis for a homodimeric ATPase subunit of an ECF transporter.Protein Cell. 2013 Oct;4(10):793-801.

11. Hao W, Collier SM, Moffett P, Chai J.Structural basis for the interaction between the potato virus X resistance protein (Rx) and its cofactor Ran GTPase-activating protein 2 (RanGAP2).J Biol Chem. 2013 Dec 13;288(50):35868-76.

12. Liu, P., Hu, Z., Zhou, B., Liu, S., and Chai, J. (2013). Crystal structure of an LRR protein with two solenoids. Cell Res.

13. Yang, H., Han, Z., Cao, Y., Fan, D., Li, H., Mo, H., Feng, Y., Liu, L., Wang, Z., Yue, Y., Chai, J.,et al. (2012). A companion cell-dominant and developmentally regulated H3K4 demethylase controls flowering time in Arabidopsis via the repression of FLC expression. PLoS Genet 8, e1002664.

14. Yuan, W., Wu, T., Fu, H., Dai, C., Wu, H., Liu, N., Li, X., Xu, M., Zhang, Z., Niu, T., et al. Chai, J. (2012). Dense chromatin activates Polycomb repressive complex 2 to regulate H3 lysine 27 methylation. Science 337, 971-975.

15. Liu, T., Liu, Z., Song, C., Hu, Y., Han, Z., She, J., Fan, F., Wang, J., Jin, C., Chang, J., et al. Chai, J. (2012). Chitin-induced dimerization activates a plant immune receptor. Science 336, 1160-1164. 

16. Gao, H., Wu, X., Chai, J., and Han, Z. (2012). Crystal structure of a TALE protein reveals an extended N-terminal DNA binding region. Cell Res 22, 1716-1720.

17. Cheng, W., Yin, K., Lu, D., Li, B., Zhu, D., Chen, Y., Zhang, H., Xu, S., Chai, J., and Gu, L. (2012). Structural insights into a unique Legionella pneumophila effector LidA recognizing both GDP and GTP bound Rab1 in their active state. PLoS Pathog 8, e1002528.

18. Bai, S., Liu, J., Chang, C., Zhang, L., Maekawa, T., Wang, Q., Xiao, W., Liu, Y., Chai, J., Takken, F. L., et al. (2012). Structure-function analysis of barley NLR immune receptor MLA10 reveals its cell compartment specific activity in cell death and disease resistance. PLoS Pathog 8, e1002752.

19. She, J., Han, Z., Kim, T. W., Wang, J., Cheng, W., Chang, J., Shi, S., Wang, J., Yang, M., Wang, Z. Y., and Chai, J. (2011). Structural insight into brassinosteroid perception by BRI1. Nature 474, 472-476.  

20. Pei, Q., Christofferson, A., Zhang, H., Chai, J., and Huang, N. (2011). Computational investigation of the enzymatic mechanisms of phosphothreonine lyase. Biophys Chem 157, 16-23.

21. Maekawa, T., Cheng, W., Spiridon, L. N., Toller, A., Lukasik, E., Saijo, Y., Liu, P., Shen, Q. H., Micluta, M. A., Somssich, I. E., et al. Chai, J. (2011). Coiled-coil domain-dependent homodimerization of intracellular barley immune receptors defines a minimal functional module for triggering cell death. Cell Host Microbe 9, 187-199.

22. Cheng, W., Munkvold, K. R., Gao, H., Mathieu, J., Schwizer, S., Wang, S., Yan, Y. B., Wang, J., Martin, G. B., and Chai, J. (2011). Structural analysis of Pseudomonas syringae AvrPtoB bound to host BAK1 reveals two similar kinase-interacting domains in a type III Effector. Cell Host Microbe 10, 616-626.

23. Huang, Z., and Chai, J. (2010). Mapping the selection mechanisms by bacterial GEFs. Virulence 1, 93-96.

24. Han, Z., Niu, T., Chang, J., Lei, X., Zhao, M., Wang, Q., Cheng, W., Wang, J., Feng, Y., and Chai, J. (2010b). Crystal structure of the FTO protein reveals basis for its substrate specificity. Nature 464, 1205-1209. 

25. Han, Z., Huang, N., Niu, T., and Chai, J. (2010a). A loop matters for FTO substrate selection. Protein Cell 1, 616-620.

26. Chen, D., Lei, L., Flores, R., Huang, Z., Wu, Z., Chai, J., and Zhong, G. (2010). Autoprocessing and self-activation of the secreted protease CPAF in Chlamydia-infected cells. Microb Pathog 49, 164-173.

27. Liang, P., Wang, H., Chen, H., Cui, Y., Gu, L., Chai, J., and Wang, K. (2009). Structural Insights into KChIP4a Modulation of Kv4.3 Inactivation. J Biol Chem 284, 4960-4967.

28. Huang, Z., Sutton, S. E., Wallenfang, A. J., Orchard, R. C., Wu, X., Feng, Y., Chai, J., and Alto, N. M. (2009). Structural insights into host GTPase isoform selection by a family of bacterial GEF mimics. Nat Struct Mol Biol 16, 853-860.

29. Dong, J., Xiao, F., Fan, F., Gu, L., Cang, H., Martin, G. B., and Chai, J.(2009). Crystal structure of the complex between Pseudomonas effector AvrPtoB and the tomato Pto kinase reveals both a shared and a unique interface compared with AvrPto-Pto. Plant Cell 21, 1846-1859.

30. Chen, D., Chai, J., Hart, P. J., and Zhong, G. (2009). Identifying catalytic residues in CPAF, a Chlamydia-secreted protease. Arch Biochem Biophys 485, 16-23.

31. Zong, N., Xiang, T., Zou, Y., Chai, J., and Zhou, J. M. (2008). Blocking and triggering of plant immunity by Pseudomonas syringae effector AvrPto. Plant Signal Behav 3, 583-585.

32. Zhou, J. M., and Chai, J. (2008). Plant pathogenic bacterial type III effectors subdue host responses. Curr Opin Microbiol 11, 179-185.

33. Xiang, T., Zong, N., Zou, Y., Wu, Y., Zhang, J., Xing, W., Li, Y., Tang, X., Zhu, L., Chai, J., and Zhou, J. M. (2008). Pseudomonas syringae effector AvrPto blocks innate immunity by targeting receptor kinases. Curr Biol 18, 74-80.

34. Ohlson, M. B., Huang, Z., Alto, N. M., Blanc, M. P., Dixon, J. E., Chai, J., and Miller, S. I. (2008). Structure and function of Salmonella SifA indicate that its interactions with SKIP, SseJ, and RhoA family GTPases induce endosomal tubulation. Cell Host Microbe 4, 434-446.

35. Huang, Z., Feng, Y., Chen, D., Wu, X., Huang, S., Wang, X., Xiao, X., Li, W., Huang, N., Gu, L., et al. Chai, J. (2008). Structural basis for activation and inhibition of the secreted chlamydia protease CPAF. Cell Host Microbe 4, 529-542.

36. Chen, L., Wang, H., Zhang, J., Gu, L., Huang, N., Zhou, J. M., and Chai, J. (2008). Structural basis for the catalytic mechanism of phosphothreonine lyase. Nat Struct Mol Biol 15, 101-102.

37. Zhifu Han, P. L., LichuanGu, Yin Zhang, Hong Li, She Chen, Jijie Chai(2007). Structural basis for histone demethylation by JHDM1 Frontier Science 1, 52-67.

38. Zhang, J., Shao, F., Li, Y., Cui, H., Chen, L., Li, H., Zou, Y., Long, C., Lan, L., Chai, J., et al. (2007). A Pseudomonas syringae effector inactivates MAPKs to suppress PAMP-induced immunity in plants. Cell Host Microbe 1, 175-185.

39. Xing, W., Zou, Y., Liu, Q., Liu, J., Luo, X., Huang, Q., Chen, S., Zhu, L., Bi, R., Hao, Q., et al. Chai, J.(2007). The structural basis for activation of plant immunity by bacterial effector protein AvrPto. Nature 449, 243-247.

40. Wang, H., Yan, Y., Liu, Q., Huang, Y., Shen, Y., Chen, L., Chen, Y., Yang, Q., Hao, Q., Wang, K., and Chai, J. (2007). Structural basis for modulation of Kv4 K+ channels by auxiliary KChIP subunits. Nat Neurosci 10, 32-39.

41. Han, Z., Xing, X., Hu, M., Zhang, Y., Liu, P., and Chai, J. (2007). Structural basis of EZH2 recognition by EED. Structure 15, 1306-1315.

42. Zhang, T., Sun, Y., Tian, E., Deng, H., Zhang, Y., Luo, X., Cai, Q., Wang, H., Chai, J., and Zhang, H. (2006). RNA-binding proteins SOP-2 and SOR-1 form a novel PcG-like complex in C. elegans. Development 133, 1023-1033.

43. Han, Z., Guo, L., Wang, H., Shen, Y., Deng, X. W., and Chai, J. (2006). Structural basis for the specific recognition of methylated histone H3 lysine 4 by the WD-40 protein WDR5. Mol Cell 22, 137-144.


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